ID A0A068S7K7_9FUNG Unreviewed; 469 AA.
AC A0A068S7K7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=carboxypeptidase C {ECO:0000256|ARBA:ARBA00012446};
DE EC=3.4.16.5 {ECO:0000256|ARBA:ARBA00012446};
GN ORFNames=LCOR_08842.1 {ECO:0000313|EMBL:CDH57960.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57960.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH57960.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDH57960.1}.
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DR EMBL; CBTN010000051; CDH57960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S7K7; -.
DR STRING; 1263082.A0A068S7K7; -.
DR VEuPathDB; FungiDB:LCOR_08842.1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.410; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:CDH57960.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..469
FT /note="carboxypeptidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001655890"
SQ SEQUENCE 469 AA; 52870 MW; FCB596C1C990D740 CRC64;
MARFALARAT LFSFVCSYWN LVLAAPSSSP SFTPKSFLSI SHPTLPEYFI RLTQPDAEIC
DPSVTQYSGY LDEPAKDKHF FFWFFESRNN PETDPLVLWL NGGPGCSSMT GLFMELGPCL
LNQDGSGTDF NPYSWNNNAS VIFLDQPVNV GYSYGPDQVH DTDSAAEDVY AFLQLFFSQF
PDAGHYIPAI GKRLVQKDAS NIQLKSLLVG NGLVDPLIQY GYYAPMVCDN HEALGLIDDQ
TCGMMKDAYP MCKNLISMCY DNPANTKVCV AASDFCNFAL LEPYYTQSGR SPYDIRKDCS
QVDDSLCDYH LSLLQDYLNR DDIKGAIIGA ADVTQRTATQ SNSTTYANCN IHINYMFQKA
GDWMRPYVRD LKALLDDHQL RVLVYAGDQD FICNWLGNKA WTMELEWHDQ EAWRSAPDLE
WGNNAGQLRT SPDGQFAFLR VYGAGHMTPA DQPENSLEFF NAWIQERLN
//
